This study will attempt to determine whether glycoproteins and glycopeptides of malignant human lymphoid cells differ from those of normal lymphocytes. The experiments will characterize the structure of the glycoproteins of the plasma membranes of two types of human lymphoma cells and cancer cells and compare them with those of normal human tonsil lymphocytes. This will be accomplished in four stages: 1. Development of a method to isolate plasma membranes in large quantities from human tonsil lymphocytes, poorly differentiated lymphocytic lymphoma cells, and well differentiated lymphocytic lymphoma cells. Carcinoma and sarcoma cells will also be studied. 2. Solubilization of the glycoprotiens of the plasma membranes and resolution by affinity chromatography on agglutinin-Sepharose columns. 3. Production of glycopeptides from purified glycoproteins by protease treatment. 4. Structural analysis of purified glycopeptides by accepted carbohydrate techniques. Additional experiments will assess quantitatively and qualitatively the biochemical processes within the lymphocytes that are coupled to two different surface glycoproteins. Agaricus bisporus agglutinin will be used to stimulate processes coupled to glycoproteins containing O-glycosidically linked oligosaccharides, and Phaseolus vulgaris phytohemagglutinin to stimulate those ccontaining N-linked receptors. Amino acid and nucleotide transport and kinetics, protein synthesis and phosphorylation, lipid phosphorylation, plasma membrane phosphorylation, RNA synthesis and RNA species distribution will be compared in short term lymphocyte cultures. Processes possibly mediating growth control will be identified.